14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport

@article{Brunet20021433TT,
  title={14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport},
  author={Anne Brunet and Fumihiko Kanai and Justine Stehn and Jian Xu and Dilara Sarbassova and John V. Frangioni and Sorab Nariman Dalal and James A. Decaprio and Michael Eldon Greenberg and Michael B. Yaffe},
  journal={The Journal of Cell Biology},
  year={2002},
  volume={156},
  pages={817 - 828}
}
14-3-3 proteins regulate the cell cycle and prevent apoptosis by controlling the nuclear and cytoplasmic distribution of signaling molecules with which they interact. Although the majority of 14-3-3 molecules are present in the cytoplasm, we show here that in the absence of bound ligands 14-3-3 homes to the nucleus. We demonstrate that phosphorylation of one important 14-3-3 binding molecule, the transcription factor FKHRL1, at the 14-3-3 binding site occurs within the nucleus immediately… 

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References

SHOWING 1-10 OF 44 REFERENCES

14-3-3 proteins: regulation of subcellular localization by molecular interference.

Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25.

It is indicated that the binding of 14-3-3 proteins and nuclear export regulate the intracellular localization of Cdc25, which contains multiple nuclear export sequences.

Association of the TLX-2 Homeodomain and 14-3-3η Signaling Proteins*

14-3-3η is defined as a functional modulator of the TLX-2 homeodomain transcription factor and suggested that the in vivo function of TLx-2 in neural differentiation is likely regulated by signaling mediated by 14- 3-3 ε, which shifts the predominant localization ofTLX-1 in COS cells from the cytoplasm to the nucleus.

Raf-1 Kinase and Exoenzyme S Interact with 14-3-3ζ through a Common Site Involving Lysine 49*

This work identifies the first point mutation (K49E) that dramatically disrupts 14-3-3ζ/ligand interactions and the parallel effects of this single point mutation on both Raf-1 binding and ExoS activation strongly suggest that diverse associated proteins share a common structural binding determinant on 14- 3- 3ζ.

14-3-3 proteins; bringing new definitions to scaffolding

The 14-3-3 proteins are a part of an emerging family of proteins and protein domains that bind to serine/threonine-phosphorylated residues in a context specific manner, analogous to the Src homology

CRM1 is responsible for intracellular transport mediated by the nuclear export signal

It is shown that p110 is CRM1, which is an evolutionarily conserved protein originally found as an essential nuclear protein in fission yeast and known as a likely target of LMB, which indicates that CRM 1 is an essential mediator of the NES-dependent nuclear export of proteins in eukaryotic cells.

Crystal structure of the zeta isoform of the 14-3-3 protein

The residues in the dimer interface and the putative ligand-binding surface are invariant among vertebrates, yeast and plants, suggesting a conservation of structure and function throughout the 14-3-3 family.

Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

The crystal structure of the human T-cell 14-3-3 isoform (τ) dimer at 2.6 Å resolution is reported, which creates a large, negatively charged channel which has been implicated in the binding of 14- 3-3 to protein kinase C.

Regulation of Histone Deacetylase 4 by Binding of 14-3-3 Proteins

Results demonstrate that HDAC4, a member of class II human HDACs, is localized in the cytoplasm and/or the nucleus and interacts with the 14-3-3 family of proteins that are known to bind specifically to conserved phosphoserine-containing motifs.